Chem. J. Chinese Universities ›› 2014, Vol. 35 ›› Issue (10): 2104.doi: 10.7503/cjcu20140141

• Organic Chemistry • Previous Articles     Next Articles

Construction and Functional Detection of Mutant Plasmid EMMPRIN Phosphorylation

ZHAO Chaoyue1, WANG Na2, WANG Juanjing2, HE Xi1, LI Jiang1,*()   

  1. 1. Department of Prothodontics, Stomatology Hospital, Jilin University, Changchun 130021, China
    2. School of Life Sciences, Northeast Normal University, Changchun 130024, China
  • Received:2014-02-25 Online:2014-10-10 Published:2014-09-30
  • Contact: LI Jiang E-mail:ljiang@jlu.edu.cn
  • Supported by:
    Supported by the Science and Technology Development Fund of Jilin Province, China(No.YYZX201241), the Natural Science Foundation of Jilin Province, China(No.201115106) and Changchun Municipal Science and Technology Bureau, China(No.2011122)

Abstract:

In order to investigate whether the proliferation of tumor cells associated with the mutant EMMPRIN phosphorylation site plasmid constructed by mutating the 246th, the 252th serine to alanine in the sequence of extracellular matrix metalloproteinase inducer, two extracellular matrix metalloproteinase inducer(EMMPRIN) phosphorylation sites were found out and mutated to construct the mutant EMMPRIN phosphorylation site plasmid with PCR site-directed mutagenesis techniques, and then to demonstrate the plasmid could be normally expressed within the cell through functional detection. The results revealed that the mutant-type EMMPRIN inhibits the proliferation of tumor cells(*P<0.05), which demonstrate that EMMPRIN may be associated with the proliferation of tumor cells.

Key words: Extracellular matrix metalloproteinase inducer(EMMPRIN), Point mutation, Phosphorylation(Ed.: P, H, N, K)

CLC Number: 

TrendMD: